| Literature DB >> 9849893 |
J K Rao1, G Bujacz, A Wlodawer.
Abstract
The crystal structure of rabbit muscle creatine kinase, solved at 2.35 A resolution by X-ray diffraction methods, clearly identified the active site with bound sulfates surrounded by a constellation of arginine residues. The putative binding site of creatine, which is occupied by a sulfate group in this analysis, has been tentatively identified. The dimeric interface of the enzyme is held together by a small number of hydrogen bonds.Entities:
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Year: 1998 PMID: 9849893 DOI: 10.1016/s0014-5793(98)01355-6
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124